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Crystal structure of the human roralpha ligand binding domain in complex with cholesterol sulfate at 2.2A

Analyse Crystal structure of the human roralpha ligand binding domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S0X
Type: protein
Length: 251 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-alpha
UniProt: P35398
Ligands: C3S
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-alpha	protein	251	74% helix, 4% strand	P35398

Ligands and binding sites

C3S · Cholest-5-en-3-yl hydrogen sulfate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	385	0.85	0.93	40	C3S
2	57	0.30	0.76	19	empty

Compared structures

1S0X · Crystal structure of the human RORalpha ligand binding domain in complex with cholesterol… · the same entry in another collection · chain A against A, TM-score 1.00
P35398 · AlphaFold monomer V2.0 prediction for nuclear receptor ror-alpha (P35398) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P35398
Elsewhere: RCSB PDB 1S0X · PDBe 1S0X · UniProt P35398

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